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HEADER HYDROLASE 30-JAN-13 4J0G
TITLE TANNIN ACYL HYDROLASE (MERCURY DERIVATIVE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANNASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;
SOURCE 3 ORGANISM_TAXID: 1590;
SOURCE 4 GENE: TANLPL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TANNIN, HYDROLASE, HYDROLYSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR B.REN,M.WU,Q.WANG,X.PENG,H.WEN,Q.CHEN,W.J.MCKINSTRY
REVDAT 1 22-MAY-13 4J0G 0
JRNL AUTH B.REN,M.WU,Q.WANG,X.PENG,H.WEN,W.J.MCKINSTRY,Q.CHEN
JRNL TITL CRYSTAL STRUCTURE OF TANNASE FROM LACTOBACILLUS PLANTARUM
JRNL REF J.MOL.BIOL. 2013
JRNL REFN ESSN 1089-8638
JRNL PMID 23648840
JRNL DOI 10.1016/J.JMB.2013.04.032
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 29147
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1452
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.7682 - 5.3538 0.95 2678 160 0.1940 0.2028
REMARK 3 2 5.3538 - 4.2635 0.97 2763 121 0.1548 0.1961
REMARK 3 3 4.2635 - 3.7287 0.97 2775 143 0.1647 0.2012
REMARK 3 4 3.7287 - 3.3896 0.98 2786 152 0.1828 0.2073
REMARK 3 5 3.3896 - 3.1477 0.98 2780 148 0.1921 0.2539
REMARK 3 6 3.1477 - 2.9628 0.98 2780 136 0.2028 0.2504
REMARK 3 7 2.9628 - 2.8148 0.98 2811 131 0.2029 0.2574
REMARK 3 8 2.8148 - 2.6926 0.98 2811 139 0.2193 0.2560
REMARK 3 9 2.6926 - 2.5892 0.98 2746 151 0.2186 0.2916
REMARK 3 10 2.5892 - 2.5000 0.97 2765 171 0.2353 0.3193
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 40.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.770
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.66820
REMARK 3 B22 (A**2) : -4.58160
REMARK 3 B33 (A**2) : 3.66490
REMARK 3 B12 (A**2) : -6.67710
REMARK 3 B13 (A**2) : 15.57740
REMARK 3 B23 (A**2) : -5.20560
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 7251
REMARK 3 ANGLE : 1.382 9874
REMARK 3 CHIRALITY : 0.115 1110
REMARK 3 PLANARITY : 0.005 1289
REMARK 3 DIHEDRAL : 14.384 2574
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid 1:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0382 115.0361 87.1395
REMARK 3 T TENSOR
REMARK 3 T11: 0.1114 T22: 0.0503
REMARK 3 T33: 0.0642 T12: -0.0125
REMARK 3 T13: 0.0368 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.0242 L22: 0.0986
REMARK 3 L33: 0.0863 L12: -0.0004
REMARK 3 L13: 0.0233 L23: -0.0678
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: 0.0134 S13: 0.0029
REMARK 3 S21: -0.0261 S22: -0.0719 S23: 0.0119
REMARK 3 S31: 0.0057 S32: -0.0623 S33: -0.0281
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 52:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4548 106.1938 84.4450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0861 T22: 0.0341
REMARK 3 T33: 0.0406 T12: -0.0297
REMARK 3 T13: -0.0439 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.1118 L22: 0.1375
REMARK 3 L33: 0.0594 L12: -0.0528
REMARK 3 L13: -0.0643 L23: 0.0715
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: 0.0309 S13: 0.0157
REMARK 3 S21: 0.0236 S22: -0.0378 S23: -0.1285
REMARK 3 S31: -0.0089 S32: -0.0640 S33: 0.0186
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 128:229)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.8741 98.7443 74.0530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0595 T22: 0.0301
REMARK 3 T33: 0.0282 T12: -0.0019
REMARK 3 T13: 0.0016 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.0335 L22: 0.0448
REMARK 3 L33: 0.0572 L12: -0.0345
REMARK 3 L13: -0.0403 L23: 0.0303
REMARK 3 S TENSOR
REMARK 3 S11: 0.0325 S12: 0.0369 S13: -0.0023
REMARK 3 S21: -0.0077 S22: -0.0288 S23: -0.0585
REMARK 3 S31: -0.0732 S32: 0.0189 S33: 0.0056
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 248:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0821 78.4886 61.5101
REMARK 3 T TENSOR
REMARK 3 T11: 0.1166 T22: 0.0149
REMARK 3 T33: 0.0620 T12: 0.0184
REMARK 3 T13: -0.0277 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.0421 L22: 0.0378
REMARK 3 L33: 0.0125 L12: 0.0386
REMARK 3 L13: 0.0101 L23: 0.0117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0459 S12: -0.0113 S13: 0.0048
REMARK 3 S21: -0.0512 S22: 0.0151 S23: 0.0378
REMARK 3 S31: 0.0073 S32: 0.0179 S33: -0.0388
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain A and resid 283:461)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2744 84.6925 71.4366
REMARK 3 T TENSOR
REMARK 3 T11: 0.0922 T22: 0.0143
REMARK 3 T33: -0.0818 T12: -0.0013
REMARK 3 T13: 0.0477 T23: -0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 0.1115 L22: 0.0652
REMARK 3 L33: 0.0829 L12: -0.0244
REMARK 3 L13: 0.0047 L23: 0.0015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0509 S12: 0.0743 S13: 0.1580
REMARK 3 S21: 0.1043 S22: -0.0173 S23: -0.0891
REMARK 3 S31: -0.0070 S32: 0.0112 S33: -0.0273
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain A and resid 462:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6992 92.7274 93.6211
REMARK 3 T TENSOR
REMARK 3 T11: 0.2488 T22: 0.1714
REMARK 3 T33: 0.1725 T12: -0.0915
REMARK 3 T13: 0.0469 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 0.0010 L22: 0.0013
REMARK 3 L33: 0.0001 L12: -0.0012
REMARK 3 L13: 0.0000 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: -0.0151 S13: -0.0017
REMARK 3 S21: 0.0170 S22: -0.0135 S23: -0.0291
REMARK 3 S31: 0.0109 S32: 0.0407 S33: 0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain B and resid 1:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7492 35.0398 28.0505
REMARK 3 T TENSOR
REMARK 3 T11: 0.0824 T22: 0.0524
REMARK 3 T33: 0.0602 T12: -0.0231
REMARK 3 T13: 0.0312 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.0647 L22: 0.0237
REMARK 3 L33: 0.1265 L12: 0.0150
REMARK 3 L13: -0.0183 L23: -0.0477
REMARK 3 S TENSOR
REMARK 3 S11: -0.0233 S12: 0.0480 S13: -0.0792
REMARK 3 S21: -0.0295 S22: -0.0232 S23: 0.0129
REMARK 3 S31: 0.0792 S32: 0.0279 S33: -0.0117
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain B and resid 52:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1200 44.5156 29.2298
REMARK 3 T TENSOR
REMARK 3 T11: 0.0312 T22: 0.0666
REMARK 3 T33: 0.0490 T12: -0.0094
REMARK 3 T13: 0.0042 T23: -0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.1990 L22: 0.0377
REMARK 3 L33: 0.0537 L12: 0.0049
REMARK 3 L13: -0.0863 L23: -0.0102
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: 0.1111 S13: 0.0440
REMARK 3 S21: -0.0635 S22: 0.0381 S23: -0.0327
REMARK 3 S31: -0.0108 S32: -0.0265 S33: 0.0246
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (chain B and resid 128:234)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8981 51.5114 40.9122
REMARK 3 T TENSOR
REMARK 3 T11: -0.0406 T22: 0.0393
REMARK 3 T33: 0.0631 T12: 0.0342
REMARK 3 T13: -0.0025 T23: 0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 0.0506 L22: 0.0656
REMARK 3 L33: 0.0138 L12: -0.0418
REMARK 3 L13: 0.0118 L23: 0.0284
REMARK 3 S TENSOR
REMARK 3 S11: 0.0061 S12: -0.0627 S13: -0.0580
REMARK 3 S21: -0.0528 S22: 0.0005 S23: 0.0092
REMARK 3 S31: 0.0115 S32: -0.0492 S33: 0.0318
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (chain B and resid 242:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4406 71.4078 45.0298
REMARK 3 T TENSOR
REMARK 3 T11: -0.0108 T22: 0.0799
REMARK 3 T33: 0.1306 T12: -0.0034
REMARK 3 T13: 0.0387 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 0.0184 L22: 0.0582
REMARK 3 L33: 0.0355 L12: -0.0261
REMARK 3 L13: -0.0242 L23: 0.0317
REMARK 3 S TENSOR
REMARK 3 S11: -0.0049 S12: -0.0235 S13: 0.0620
REMARK 3 S21: -0.0221 S22: 0.0369 S23: -0.0279
REMARK 3 S31: -0.0019 S32: 0.0194 S33: 0.0138
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (chain B and resid 283:461)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3204 66.5886 40.3832
REMARK 3 T TENSOR
REMARK 3 T11: -0.2961 T22: 0.0193
REMARK 3 T33: -0.0642 T12: -0.0945
REMARK 3 T13: 0.2162 T23: 0.0456
REMARK 3 L TENSOR
REMARK 3 L11: 0.1585 L22: 0.1350
REMARK 3 L33: 0.0563 L12: -0.0291
REMARK 3 L13: -0.0042 L23: 0.0046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0146 S12: 0.0525 S13: 0.0469
REMARK 3 S21: -0.0977 S22: 0.0871 S23: -0.0406
REMARK 3 S31: -0.0358 S32: -0.0063 S33: 0.0335
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (chain B and resid 462:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.7434 53.3840 32.2418
REMARK 3 T TENSOR
REMARK 3 T11: 0.1129 T22: 0.1442
REMARK 3 T33: 0.1224 T12: 0.0037
REMARK 3 T13: 0.0225 T23: 0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 0.0054 L22: 0.0020
REMARK 3 L33: 0.0011 L12: -0.0013
REMARK 3 L13: 0.0023 L23: -0.0007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0125 S12: -0.0005 S13: -0.0011
REMARK 3 S21: 0.0029 S22: -0.0046 S23: -0.0225
REMARK 3 S31: 0.0042 S32: 0.0217 S33: 0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4J0G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-13.
REMARK 100 THE RCSB ID CODE IS RCSB077439.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25246
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.23300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE PH 5.5, 20%
REMARK 280 PEG 3000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN A 230
REMARK 465 PRO A 231
REMARK 465 VAL A 232
REMARK 465 ALA A 233
REMARK 465 GLY A 234
REMARK 465 THR A 235
REMARK 465 THR A 236
REMARK 465 LYS A 237
REMARK 465 ASN A 238
REMARK 465 GLY A 239
REMARK 465 ARG A 240
REMARK 465 PRO A 241
REMARK 465 LYS A 242
REMARK 465 PHE A 243
REMARK 465 GLU A 244
REMARK 465 PRO A 245
REMARK 465 THR B 235
REMARK 465 THR B 236
REMARK 465 LYS B 237
REMARK 465 ASN B 238
REMARK 465 GLY B 239
REMARK 465 ARG B 240
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LEU A 269 CA CB CG CD1 CD2
REMARK 480 SER B 266 CA CB OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TYR A 268 NE2 GLN A 271 1.89
REMARK 500 O HOH A 689 O HOH A 710 1.93
REMARK 500 O GLY B 123 O HOH B 624 1.99
REMARK 500 OD1 ASP A 278 OG1 THR A 280 2.06
REMARK 500 O PRO A 72 O HOH A 710 2.13
REMARK 500 O HOH B 641 O HOH B 721 2.14
REMARK 500 OD2 ASP B 456 O HOH B 616 2.15
REMARK 500 O HOH A 668 O HOH A 708 2.16
REMARK 500 O HOH A 675 O HOH A 721 2.16
REMARK 500 OD2 ASP A 421 O HOH A 740 2.17
REMARK 500 OE1 GLU A 182 O HOH A 701 2.18
REMARK 500 O GLY A 362 O HOH A 704 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2 GLN A 63 O LYS B 316 1556 1.59
REMARK 500 OD2 ASP B 153 OH2 1PE B 503 1655 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 339 CB - CG - CD1 ANGL. DEV. = -10.4 DEGREES
REMARK 500 CYS B 468 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 20 103.50 -48.11
REMARK 500 PRO A 130 38.12 -99.59
REMARK 500 SER A 163 -125.06 66.54
REMARK 500 CYS A 204 58.45 33.72
REMARK 500 ARG A 228 -156.49 -146.96
REMARK 500 THR A 340 -146.31 76.33
REMARK 500 PRO B 130 39.86 -99.42
REMARK 500 SER B 163 -126.45 67.04
REMARK 500 ARG B 228 -156.05 -145.64
REMARK 500 THR B 340 -169.53 72.23
REMARK 500 PHE B 348 -56.23 -120.48
REMARK 500 THR B 365 -60.90 -97.05
REMARK 500 LEU B 445 75.53 -113.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP B 454 TYR B 455 140.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLN A 22 17.9 L L OUTSIDE RANGE
REMARK 500 SER A 58 23.5 L L OUTSIDE RANGE
REMARK 500 ASP A 448 24.3 L L OUTSIDE RANGE
REMARK 500 GLN A 469 24.4 L L OUTSIDE RANGE
REMARK 500 HIS B 55 20.0 L L OUTSIDE RANGE
REMARK 500 THR B 280 24.7 L L OUTSIDE RANGE
REMARK 500 ARG B 341 20.9 L L OUTSIDE RANGE
REMARK 500 LYS B 409 24.1 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B 502 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 204 SG
REMARK 620 2 ASP B 419 OD2 78.8
REMARK 620 3 HOH B 743 O 175.5 100.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 502 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 204 SG
REMARK 620 2 ASP A 419 OD2 74.0
REMARK 620 3 ASP A 421 OD2 102.2 125.5
REMARK 620 4 HOH A 740 O 82.1 150.9 44.1
REMARK 620 5 HOH A 739 O 168.5 96.7 77.4 104.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 501 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 468 SG
REMARK 620 2 CYS A 468 O 74.7
REMARK 620 3 HOH A 737 O 148.8 81.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 507
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4J0C RELATED DB: PDB
REMARK 900 RELATED ID: 4J0D RELATED DB: PDB
REMARK 900 RELATED ID: 4J0H RELATED DB: PDB
REMARK 900 RELATED ID: 4J0I RELATED DB: PDB
REMARK 900 RELATED ID: 4J0J RELATED DB: PDB
REMARK 900 RELATED ID: 4J0K RELATED DB: PDB
REMARK 900 RELATED ID: 4JUI RELATED DB: PDB
DBREF 4J0G A 1 469 UNP B3Y018 B3Y018_LACPN 1 469
DBREF 4J0G B 1 469 UNP B3Y018 B3Y018_LACPN 1 469
SEQADV 4J0G SER A 0 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0G SER B 0 UNP B3Y018 EXPRESSION TAG
SEQRES 1 A 470 SER MET SER ASN ARG LEU ILE PHE ASP ALA ASP TRP LEU
SEQRES 2 A 470 VAL PRO GLU GLN VAL GLN VAL ALA GLY GLN ALA ILE GLN
SEQRES 3 A 470 TYR TYR ALA ALA ARG ASN ILE GLN TYR VAL GLN HIS PRO
SEQRES 4 A 470 VAL ALA ALA ILE GLN VAL LEU ASN VAL PHE VAL PRO ALA
SEQRES 5 A 470 ALA TYR LEU HIS GLY SER SER VAL ASN GLY TYR GLN ARG
SEQRES 6 A 470 ALA THR ALA PRO ILE LEU MET PRO ASN THR VAL GLY GLY
SEQRES 7 A 470 TYR LEU PRO GLY PRO ALA ASP ASP PRO GLN ARG VAL THR
SEQRES 8 A 470 TRP PRO THR ASN ALA GLY THR ILE GLN GLN ALA LEU LYS
SEQRES 9 A 470 ARG GLY TYR VAL VAL VAL ALA ALA GLY ILE ARG GLY ARG
SEQRES 10 A 470 THR THR VAL ASP LYS SER GLY GLN ARG VAL GLY GLN ALA
SEQRES 11 A 470 PRO ALA PHE ILE VAL ASP MET LYS ALA ALA ILE ARG TYR
SEQRES 12 A 470 VAL LYS TYR ASN GLN GLY ARG LEU PRO GLY ASP ALA ASN
SEQRES 13 A 470 ARG ILE ILE THR ASN GLY THR SER ALA GLY GLY ALA THR
SEQRES 14 A 470 SER ALA LEU ALA GLY ALA SER GLY ASN SER ALA TYR PHE
SEQRES 15 A 470 GLU PRO ALA LEU THR ALA LEU GLY ALA ALA PRO ALA THR
SEQRES 16 A 470 ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO ILE HIS
SEQRES 17 A 470 ASN LEU GLU HIS ALA ASP MET ALA TYR GLU TRP GLN PHE
SEQRES 18 A 470 ASN GLY ILE ASN ASP TRP HIS ARG TYR GLN PRO VAL ALA
SEQRES 19 A 470 GLY THR THR LYS ASN GLY ARG PRO LYS PHE GLU PRO VAL
SEQRES 20 A 470 SER GLY GLN LEU THR VAL GLU GLU GLN ALA LEU SER LEU
SEQRES 21 A 470 ALA LEU LYS ALA GLN PHE SER THR TYR LEU ASN GLN LEU
SEQRES 22 A 470 LYS LEU THR ALA SER ASP GLY THR HIS LEU THR LEU ASN
SEQRES 23 A 470 GLU ALA GLY MET GLY SER PHE ARG ASP VAL VAL ARG GLN
SEQRES 24 A 470 LEU LEU ILE SER SER ALA GLN THR ALA PHE ASP GLN GLY
SEQRES 25 A 470 THR ASP ILE HIS LYS TYR ALA GLY PHE VAL VAL THR GLY
SEQRES 26 A 470 ASN GLN VAL THR ASP LEU ASP LEU SER ALA TYR LEU LYS
SEQRES 27 A 470 SER LEU THR ARG MET LYS ALA VAL PRO ALA PHE ASP GLN
SEQRES 28 A 470 LEU ASP LEU THR SER PRO GLU ASN ASN LEU PHE GLY ASP
SEQRES 29 A 470 ALA THR ALA LYS ALA LYS HIS PHE THR ALA LEU ALA GLN
SEQRES 30 A 470 THR ARG SER THR VAL THR ALA GLN LEU ALA ASP ALA GLU
SEQRES 31 A 470 LEU ILE GLN ALA ILE ASN PRO LEU SER TYR LEU THR THR
SEQRES 32 A 470 THR SER SER GLN VAL ALA LYS HIS TRP ARG ILE ARG HIS
SEQRES 33 A 470 GLY ALA ALA ASP ARG ASP THR SER PHE ALA ILE PRO ILE
SEQRES 34 A 470 ILE LEU ALA ILE MET LEU GLU ASN HIS GLY TYR GLY ILE
SEQRES 35 A 470 ASP PHE ALA LEU PRO TRP ASP ILE PRO HIS SER GLY ASP
SEQRES 36 A 470 TYR ASP LEU GLY ASP LEU PHE SER TRP ILE ASP GLY LEU
SEQRES 37 A 470 CYS GLN
SEQRES 1 B 470 SER MET SER ASN ARG LEU ILE PHE ASP ALA ASP TRP LEU
SEQRES 2 B 470 VAL PRO GLU GLN VAL GLN VAL ALA GLY GLN ALA ILE GLN
SEQRES 3 B 470 TYR TYR ALA ALA ARG ASN ILE GLN TYR VAL GLN HIS PRO
SEQRES 4 B 470 VAL ALA ALA ILE GLN VAL LEU ASN VAL PHE VAL PRO ALA
SEQRES 5 B 470 ALA TYR LEU HIS GLY SER SER VAL ASN GLY TYR GLN ARG
SEQRES 6 B 470 ALA THR ALA PRO ILE LEU MET PRO ASN THR VAL GLY GLY
SEQRES 7 B 470 TYR LEU PRO GLY PRO ALA ASP ASP PRO GLN ARG VAL THR
SEQRES 8 B 470 TRP PRO THR ASN ALA GLY THR ILE GLN GLN ALA LEU LYS
SEQRES 9 B 470 ARG GLY TYR VAL VAL VAL ALA ALA GLY ILE ARG GLY ARG
SEQRES 10 B 470 THR THR VAL ASP LYS SER GLY GLN ARG VAL GLY GLN ALA
SEQRES 11 B 470 PRO ALA PHE ILE VAL ASP MET LYS ALA ALA ILE ARG TYR
SEQRES 12 B 470 VAL LYS TYR ASN GLN GLY ARG LEU PRO GLY ASP ALA ASN
SEQRES 13 B 470 ARG ILE ILE THR ASN GLY THR SER ALA GLY GLY ALA THR
SEQRES 14 B 470 SER ALA LEU ALA GLY ALA SER GLY ASN SER ALA TYR PHE
SEQRES 15 B 470 GLU PRO ALA LEU THR ALA LEU GLY ALA ALA PRO ALA THR
SEQRES 16 B 470 ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO ILE HIS
SEQRES 17 B 470 ASN LEU GLU HIS ALA ASP MET ALA TYR GLU TRP GLN PHE
SEQRES 18 B 470 ASN GLY ILE ASN ASP TRP HIS ARG TYR GLN PRO VAL ALA
SEQRES 19 B 470 GLY THR THR LYS ASN GLY ARG PRO LYS PHE GLU PRO VAL
SEQRES 20 B 470 SER GLY GLN LEU THR VAL GLU GLU GLN ALA LEU SER LEU
SEQRES 21 B 470 ALA LEU LYS ALA GLN PHE SER THR TYR LEU ASN GLN LEU
SEQRES 22 B 470 LYS LEU THR ALA SER ASP GLY THR HIS LEU THR LEU ASN
SEQRES 23 B 470 GLU ALA GLY MET GLY SER PHE ARG ASP VAL VAL ARG GLN
SEQRES 24 B 470 LEU LEU ILE SER SER ALA GLN THR ALA PHE ASP GLN GLY
SEQRES 25 B 470 THR ASP ILE HIS LYS TYR ALA GLY PHE VAL VAL THR GLY
SEQRES 26 B 470 ASN GLN VAL THR ASP LEU ASP LEU SER ALA TYR LEU LYS
SEQRES 27 B 470 SER LEU THR ARG MET LYS ALA VAL PRO ALA PHE ASP GLN
SEQRES 28 B 470 LEU ASP LEU THR SER PRO GLU ASN ASN LEU PHE GLY ASP
SEQRES 29 B 470 ALA THR ALA LYS ALA LYS HIS PHE THR ALA LEU ALA GLN
SEQRES 30 B 470 THR ARG SER THR VAL THR ALA GLN LEU ALA ASP ALA GLU
SEQRES 31 B 470 LEU ILE GLN ALA ILE ASN PRO LEU SER TYR LEU THR THR
SEQRES 32 B 470 THR SER SER GLN VAL ALA LYS HIS TRP ARG ILE ARG HIS
SEQRES 33 B 470 GLY ALA ALA ASP ARG ASP THR SER PHE ALA ILE PRO ILE
SEQRES 34 B 470 ILE LEU ALA ILE MET LEU GLU ASN HIS GLY TYR GLY ILE
SEQRES 35 B 470 ASP PHE ALA LEU PRO TRP ASP ILE PRO HIS SER GLY ASP
SEQRES 36 B 470 TYR ASP LEU GLY ASP LEU PHE SER TRP ILE ASP GLY LEU
SEQRES 37 B 470 CYS GLN
HET HG A 501 1
HET HG A 502 1
HET PEG A 503 7
HET PEG A 504 7
HET PEG A 505 7
HET HG B 501 1
HET HG B 502 1
HET 1PE B 503 16
HET PEG B 504 7
HET PEG B 505 7
HET PEG B 506 7
HET PEG B 507 7
HETNAM HG MERCURY (II) ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 HG 4(HG 2+)
FORMUL 5 PEG 7(C4 H10 O3)
FORMUL 10 1PE C10 H22 O6
FORMUL 15 HOH *326(H2 O)
HELIX 1 1 ASP A 8 LEU A 12 5 5
HELIX 2 2 ALA A 52 HIS A 55 5 4
HELIX 3 3 ASN A 94 GLY A 105 1 12
HELIX 4 4 PRO A 130 ASN A 146 1 17
HELIX 5 5 SER A 163 SER A 175 1 13
HELIX 6 6 SER A 178 TYR A 180 5 3
HELIX 7 7 PHE A 181 GLY A 189 1 9
HELIX 8 8 ASN A 208 ASN A 221 1 14
HELIX 9 9 THR A 251 GLN A 271 1 21
HELIX 10 10 GLY A 290 GLN A 310 1 21
HELIX 11 11 ASP A 313 TYR A 317 5 5
HELIX 12 12 ASP A 331 THR A 340 1 10
HELIX 13 13 SER A 355 PHE A 361 1 7
HELIX 14 14 THR A 372 ARG A 378 1 7
HELIX 15 15 ASP A 387 ILE A 394 1 8
HELIX 16 16 ASN A 395 LEU A 400 5 6
HELIX 17 17 PHE A 424 HIS A 437 1 14
HELIX 18 18 ASP A 456 GLN A 469 1 14
HELIX 19 19 ASP B 8 LEU B 12 5 5
HELIX 20 20 ALA B 52 HIS B 55 5 4
HELIX 21 21 ASN B 94 GLY B 105 1 12
HELIX 22 22 PRO B 130 ASN B 146 1 17
HELIX 23 23 ASP B 153 ASN B 155 5 3
HELIX 24 24 SER B 163 SER B 175 1 13
HELIX 25 25 SER B 178 TYR B 180 5 3
HELIX 26 26 PHE B 181 GLY B 189 1 9
HELIX 27 27 ASN B 208 ASN B 221 1 14
HELIX 28 28 THR B 251 LEU B 272 1 22
HELIX 29 29 GLY B 290 ASP B 309 1 20
HELIX 30 30 ASP B 331 THR B 340 1 10
HELIX 31 31 SER B 355 PHE B 361 1 7
HELIX 32 32 THR B 372 ARG B 378 1 7
HELIX 33 33 ASP B 387 ILE B 394 1 8
HELIX 34 34 ASN B 395 LEU B 400 5 6
HELIX 35 35 PHE B 424 HIS B 437 1 14
HELIX 36 36 ASP B 456 CYS B 468 1 13
SHEET 1 A 9 VAL A 13 VAL A 19 0
SHEET 2 A 9 GLN A 22 ILE A 32 -1 O GLN A 22 N VAL A 19
SHEET 3 A 9 LEU A 45 PRO A 50 -1 O VAL A 49 N TYR A 27
SHEET 4 A 9 VAL A 107 ALA A 111 -1 O VAL A 108 N PHE A 48
SHEET 5 A 9 ILE A 69 PRO A 72 1 N LEU A 70 O VAL A 107
SHEET 6 A 9 ILE A 157 ASN A 160 1 O ILE A 158 N MET A 71
SHEET 7 A 9 ALA A 199 TYR A 203 1 O SER A 201 N THR A 159
SHEET 8 A 9 HIS A 410 ARG A 414 1 O HIS A 410 N VAL A 200
SHEET 9 A 9 GLY A 440 ALA A 444 1 O ASP A 442 N ILE A 413
SHEET 1 B 2 ASP A 225 HIS A 227 0
SHEET 2 B 2 SER A 247 GLN A 249 -1 O GLY A 248 N TRP A 226
SHEET 1 C 2 PHE A 320 THR A 323 0
SHEET 2 C 2 GLN A 326 LEU A 330 -1 O GLN A 326 N THR A 323
SHEET 1 D 9 VAL B 13 VAL B 19 0
SHEET 2 D 9 GLN B 22 GLN B 33 -1 O TYR B 26 N GLU B 15
SHEET 3 D 9 VAL B 44 PRO B 50 -1 O VAL B 49 N TYR B 27
SHEET 4 D 9 VAL B 107 ALA B 111 -1 O VAL B 108 N PHE B 48
SHEET 5 D 9 ILE B 69 PRO B 72 1 N LEU B 70 O VAL B 107
SHEET 6 D 9 ILE B 157 THR B 162 1 O ILE B 158 N MET B 71
SHEET 7 D 9 ALA B 199 TYR B 203 1 O TYR B 203 N GLY B 161
SHEET 8 D 9 HIS B 410 ARG B 414 1 O ARG B 412 N ALA B 202
SHEET 9 D 9 GLY B 440 ALA B 444 1 O ASP B 442 N TRP B 411
SHEET 1 E 2 ASP B 225 VAL B 232 0
SHEET 2 E 2 LYS B 242 GLN B 249 -1 O GLU B 244 N GLN B 230
SHEET 1 F 2 PHE B 320 THR B 323 0
SHEET 2 F 2 GLN B 326 LEU B 330 -1 O GLN B 326 N THR B 323
LINK SG CYS B 204 HG HG B 502 1555 1555 2.45
LINK SG CYS A 204 HG HG A 502 1555 1555 2.56
LINK SG CYS A 468 HG HG A 501 1555 1555 2.76
LINK OD2 ASP B 419 HG HG B 502 1555 1555 2.91
LINK OD2 ASP A 419 HG HG A 502 1555 1555 2.95
LINK OD2 ASP A 421 HG HG A 502 1555 1555 3.07
LINK O CYS A 468 HG HG A 501 1555 1555 3.12
LINK HG HG B 501 O HOH B 735 1555 1555 2.49
LINK HG HG A 502 O HOH A 740 1555 1555 2.59
LINK HG HG B 502 O HOH B 743 1555 1555 2.65
LINK HG HG A 501 O HOH A 737 1555 1555 2.74
LINK HG HG A 502 O HOH A 739 1555 1555 2.87
CISPEP 1 TRP A 91 PRO A 92 0 -3.76
CISPEP 2 ALA A 129 PRO A 130 0 4.04
CISPEP 3 VAL A 345 PRO A 346 0 -9.54
CISPEP 4 TRP B 91 PRO B 92 0 -4.85
CISPEP 5 ALA B 129 PRO B 130 0 3.09
CISPEP 6 VAL B 345 PRO B 346 0 -7.60
CISPEP 7 TYR B 455 ASP B 456 0 -27.97
SITE 1 AC1 3 THR A 66 CYS A 468 HOH A 737
SITE 1 AC2 7 CYS A 204 ASP A 419 ASP A 421 HIS A 451
SITE 2 AC2 7 SER A 452 HOH A 739 HOH A 740
SITE 1 AC3 3 PRO A 86 GLN A 87 GLN A 99
SITE 1 AC4 1 ILE A 441
SITE 1 AC5 7 TRP A 218 LYS A 262 ALA A 287 GLY A 288
SITE 2 AC5 7 ARG A 293 SER A 333 LEU A 336
SITE 1 AC6 4 TYR B 62 THR B 66 CYS B 468 HOH B 735
SITE 1 AC7 4 CYS B 204 ASP B 419 ASP B 421 HOH B 743
SITE 1 AC8 15 THR A 382 GLN A 384 ALA B 65 THR B 66
SITE 2 AC8 15 SER B 122 GLY B 123 GLN B 124 ARG B 125
SITE 3 AC8 15 GLN B 147 ASP B 153 ASN B 155 ARG B 156
SITE 4 AC8 15 PEG B 504 HOH B 624 HOH B 651
SITE 1 AC9 5 ARG B 125 ARG B 156 LYS B 367 LYS B 409
SITE 2 AC9 5 1PE B 503
SITE 1 BC1 6 TRP B 218 LYS B 262 GLY B 288 ARG B 293
SITE 2 BC1 6 SER B 333 LEU B 336
SITE 1 BC2 4 ASN B 60 GLY B 61 TYR B 62 GLN B 469
SITE 1 BC3 1 GLU B 435
CRYST1 46.357 62.686 83.122 70.49 86.93 79.10 P 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.021572 -0.004154 0.000226 0.00000
SCALE2 0.000000 0.016246 -0.005683 0.00000
SCALE3 0.000000 0.000000 0.012764 0.00000
TER 3476 GLN A 469
TER 7030 GLN B 469
MASTER 626 0 12 36 26 0 19 6 7402 2 82 74
END |